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Volumn 3, Issue 4, 2008, Pages

Sorting signals, N-terminal modifications and abundance of the chloroplast proteome

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; CELL PROTEIN; CHAPERONE; CHAPERONE 10; CHAPERONE 20; CHAPERONE 60; CHAPERONE B3; CHAPERONIN; CHLOROPLAST SIGNAL REDUCTION PARTICLE SUBUNIT 43; CHLOROPLAST SIGNAL REDUCTION PARTICLE SUBUNIT 54; DEFORMYLASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; ISOMERASE; METHIONINE SULFOXIDE REDUCTASE; NUCLEOTIDE BINDING PROTEIN; PEPTIDASE; PLASTOCYANIN; PLASTOCYANIN 1; PROTEIN DNAJ; PROTEIN DNAK; PROTEIN ES; PROTEIN ROC4; PROTEIN SECA; PROTEINASE; PROTEINASE ATPREP1; PROTEINASE DEGP2; SIGNAL PEPTIDE; STROMAL PROCESSING PEPTIDASE; ARABIDOPSIS PROTEIN; CHLOROPLAST TRANSIT PEPTIDE CTP; PROTEOME;

EID: 44349099751     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001994     Document Type: Article
Times cited : (546)

References (81)
  • 1
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Hermann SG (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochemistry 80: 535-545.
    • (1989) Eur J Biochemistry , vol.80 , pp. 535-545
    • von Heijne, G.1    Steppuhn, J.2    Hermann, S.G.3
  • 2
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2(4): 953-971.
    • (2007) Nat Protoc , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 3
    • 1642276286 scopus 로고    scopus 로고
    • An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice
    • Richly E, Leister D (2004) An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice. Gene 329: 11-16.
    • (2004) Gene , vol.329 , pp. 11-16
    • Richly, E.1    Leister, D.2
  • 4
    • 3042581458 scopus 로고    scopus 로고
    • Analysis of curated and predicted plastid subproteomes of Arabidopsis. Subcellular compartmentalization leads to distinctive proteome properties
    • Sun Q, Emanuelsson O, van Wijk KJ (2004) Analysis of curated and predicted plastid subproteomes of Arabidopsis. Subcellular compartmentalization leads to distinctive proteome properties. Plant Physiol 135(2): 723-734.
    • (2004) Plant Physiol , vol.135 , Issue.2 , pp. 723-734
    • Sun, Q.1    Emanuelsson, O.2    van Wijk, K.J.3
  • 5
    • 13444267478 scopus 로고    scopus 로고
    • Plastid proteomics
    • van Wijk KJ (2004) Plastid proteomics. Plant Physiol Biochem 42(12): 963-77.
    • (2004) Plant Physiol Biochem , vol.42 , Issue.12 , pp. 963-977
    • van Wijk, K.J.1
  • 6
    • 2942530586 scopus 로고    scopus 로고
    • Chloroplast proteomics: Potentials and challenges
    • Baginsky S, Gruissem W (2004) Chloroplast proteomics: potentials and challenges. J Exp Bot 55(400): 1213-1220.
    • (2004) J Exp Bot , vol.55 , Issue.400 , pp. 1213-1220
    • Baginsky, S.1    Gruissem, W.2
  • 7
    • 33749624260 scopus 로고    scopus 로고
    • Recent surprises in protein targeting to mitochondria and plastids
    • Millar AH, Whelan J, Small I (2006) Recent surprises in protein targeting to mitochondria and plastids. Curr Opin Plant Biol 9(6): 610-615.
    • (2006) Curr Opin Plant Biol , vol.9 , Issue.6 , pp. 610-615
    • Millar, A.H.1    Whelan, J.2    Small, I.3
  • 10
    • 33646239605 scopus 로고    scopus 로고
    • Arabidopsis thaliana proteomics: From proteome to genome
    • Baginsky S, Gruissem W (2006) Arabidopsis thaliana proteomics: from proteome to genome. J Exp Bot 57(7): 1485-1491.
    • (2006) J Exp Bot , vol.57 , Issue.7 , pp. 1485-1491
    • Baginsky, S.1    Gruissem, W.2
  • 12
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood JL, Tonti-Filippini J, Verboom RE, Millar AH (2005) Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol 139(2): 598-609.
    • (2005) Plant Physiol , vol.139 , Issue.2 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 13
    • 33644896212 scopus 로고    scopus 로고
    • The role of mass spectrometry in plant systems biology
    • Glinski M, Weckwerth W (2006) The role of mass spectrometry in plant systems biology. Mass Spectrum Rev 25(2): 173-214.
    • (2006) Mass Spectrum Rev , vol.25 , Issue.2 , pp. 173-214
    • Glinski, M.1    Weckwerth, W.2
  • 15
    • 3242731195 scopus 로고    scopus 로고
    • Liu H, Sadygov RG, Yates JR 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76(14): 4193-4201.
    • Liu H, Sadygov RG, Yates JR 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76(14): 4193-4201.
  • 16
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov B, Coleman MK, Florens L, Washburn MP (2005) Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal Chem 77(19): 6218-6224.
    • (2005) Anal Chem , vol.77 , Issue.19 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4
  • 18
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu P, Vogel C, Wang F, Yao X, Marcotte EM (2007) Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25(1): 117-124.
    • (2007) Nat Biotechnol , vol.25 , Issue.1 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, F.3    Yao, X.4    Marcotte, E.M.5
  • 19
    • 17844394177 scopus 로고    scopus 로고
    • Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry
    • Listgarten J, Emili A (2005) Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 4(4): 419-434.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.4 , pp. 419-434
    • Listgarten, J.1    Emili, A.2
  • 20
    • 35848929694 scopus 로고    scopus 로고
    • Analysis and validation of proteomic data generated by tandem mass spectrometry
    • Nesvizhskii AI, Vitek O, Aebersold R (2007) Analysis and validation of proteomic data generated by tandem mass spectrometry. Nat Methods 4(10): 787-797.
    • (2007) Nat Methods , vol.4 , Issue.10 , pp. 787-797
    • Nesvizhskii, A.I.1    Vitek, O.2    Aebersold, R.3
  • 21
  • 23
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • Giglione C, Serero A, Pierre M, Boisson B, Meinnel T (2000) Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. Embo J 19(21): 5916-5929.
    • (2000) Embo J , vol.19 , Issue.21 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 24
    • 0036401120 scopus 로고    scopus 로고
    • Specificity of chloroplast-localized peptide deformylases as determined with peptide analogs of chloroplast-translated proteins
    • Dirk LM, Williams MA, Houtz RL (2002) Specificity of chloroplast-localized peptide deformylases as determined with peptide analogs of chloroplast-translated proteins. Arch Biochem Biophys 406(1): 135-141.
    • (2002) Arch Biochem Biophys , vol.406 , Issue.1 , pp. 135-141
    • Dirk, L.M.1    Williams, M.A.2    Houtz, R.L.3
  • 25
    • 0034818097 scopus 로고    scopus 로고
    • Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in Arabidopsis
    • Dirk LM, Williams MA, Houtz RL (2001) Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in Arabidopsis. Plant Physiol 127(1): 97-107.
    • (2001) Plant Physiol , vol.127 , Issue.1 , pp. 97-107
    • Dirk, L.M.1    Williams, M.A.2    Houtz, R.L.3
  • 26
    • 0035543404 scopus 로고    scopus 로고
    • Organellar peptide deformylases: Universality of the N-terminal methionine cleavage mechanism
    • Giglione C, Meinnel T (2001) Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism. Trends Plant Sci 6(12): 566-572.
    • (2001) Trends Plant Sci , vol.6 , Issue.12 , pp. 566-572
    • Giglione, C.1    Meinnel, T.2
  • 27
    • 0037413729 scopus 로고    scopus 로고
    • Control of protein life-span by N-terminal methionine excision
    • Giglione C, Vallon O, Meinnel T (2003) Control of protein life-span by N-terminal methionine excision. Embo J 22(1): 13-23.
    • (2003) Embo J , vol.22 , Issue.1 , pp. 13-23
    • Giglione, C.1    Vallon, O.2    Meinnel, T.3
  • 28
    • 19044396327 scopus 로고    scopus 로고
    • Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis
    • Ross S, Giglione C, Pierre M, Espagne C, Meinnel T (2005) Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis. Plant Physiol 137(2): 623-637.
    • (2005) Plant Physiol , vol.137 , Issue.2 , pp. 623-637
    • Ross, S.1    Giglione, C.2    Pierre, M.3    Espagne, C.4    Meinnel, T.5
  • 29
    • 33746211620 scopus 로고    scopus 로고
    • Impact of the N-terminal amino acid on targeted protein degradation
    • Meinnel T, Serero A, Giglione C (2006) Impact of the N-terminal amino acid on targeted protein degradation. Biol Chem 387(7): 839-851.
    • (2006) Biol Chem , vol.387 , Issue.7 , pp. 839-851
    • Meinnel, T.1    Serero, A.2    Giglione, C.3
  • 30
    • 33646145726 scopus 로고    scopus 로고
    • Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts
    • Adam Z, Rudella A, van Wijk KJ (2006) Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts. Curr Opin Plant Biol 9(3): 234-240.
    • (2006) Curr Opin Plant Biol , vol.9 , Issue.3 , pp. 234-240
    • Adam, Z.1    Rudella, A.2    van Wijk, K.J.3
  • 31
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen ON (2006) Interpreting the protein language using proteomics. Nat Rev Mol Cell Biol 7(6): 391-403.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.6 , pp. 391-403
    • Jensen, O.N.1
  • 32
    • 33846488609 scopus 로고    scopus 로고
    • Mass Spectrometric Mapping of Linker Historic H1 Variants Reveals Multiple Acetylations, Methylations, and Phosphorylation as Well as Differences between Cell Culture and Tissue
    • Wisniewski JR, Zougman A, Kruger S, Mann M (2007) Mass Spectrometric Mapping of Linker Historic H1 Variants Reveals Multiple Acetylations, Methylations, and Phosphorylation as Well as Differences between Cell Culture and Tissue. Mol Cell Proteomics 6(1): 72-87.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.1 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3    Mann, M.4
  • 33
    • 33750319346 scopus 로고    scopus 로고
    • Orbitrap mass analyzer - overview and applications in proteomics
    • Seigelova M, Makarov A (2006) Orbitrap mass analyzer - overview and applications in proteomics. Proteomics 6 Suppl 2: 16-21.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 2 , pp. 16-21
    • Seigelova, M.1    Makarov, A.2
  • 35
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • Olsen JV, Macek B, Lange O, Makarov A, Horning S, Mann M (2007) Higher-energy C-trap dissociation for peptide modification analysis. Nat Methods 4(9): 709-712.
    • (2007) Nat Methods , vol.4 , Issue.9 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 36
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of die thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: New proteins, new functions, and a plastid proteome database
    • Friso G, Giacomelli L, Ytterberg AJ, Peltier JB, Rudella A, Sun Q, Wijk KJ (2004) In-depth analysis of die thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Plant Cell 16(2): 478-499.
    • (2004) Plant Cell , vol.16 , Issue.2 , pp. 478-499
    • Friso, G.1    Giacomelli, L.2    Ytterberg, A.J.3    Peltier, J.B.4    Rudella, A.5    Sun, Q.6    Wijk, K.J.7
  • 37
    • 34447098784 scopus 로고    scopus 로고
    • Patterns of beauty-omics meets plant development
    • Hennig L (2007) Patterns of beauty-omics meets plant development. Trends Plant Sci 12(7): 287-293.
    • (2007) Trends Plant Sci , vol.12 , Issue.7 , pp. 287-293
    • Hennig, L.1
  • 38
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J Proteome Res 2(1): 43-50.
    • (2003) J Proteome Res , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 39
    • 0004249246 scopus 로고    scopus 로고
    • New York: W.H. FREEMAN and COMPANY
    • Sokal R, Rohlf FJJ (2005) Chapter 5 in Biometry. New York: W.H. FREEMAN and COMPANY.
    • (2005) in Biometry
    • Sokal, R.1    Rohlf, F.J.J.2
  • 45
    • 12144291195 scopus 로고    scopus 로고
    • MAPMAN: A user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes
    • Thimm O, Blasing O, Gibon Y, Nagel A, Meyer S, Kruger P, Selbig J, Muller LA, Rhee SY, Stitt M (2004) MAPMAN: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes. Plant J 37(6): 914-939.
    • (2004) Plant J , vol.37 , Issue.6 , pp. 914-939
    • Thimm, O.1    Blasing, O.2    Gibon, Y.3    Nagel, A.4    Meyer, S.5    Kruger, P.6    Selbig, J.7    Muller, L.A.8    Rhee, S.Y.9    Stitt, M.10
  • 47
    • 34250166903 scopus 로고    scopus 로고
    • Support for a potential role of E. coli oligopeptidase A in protein degradation
    • Jain R, Chan MK (2007) Support for a potential role of E. coli oligopeptidase A in protein degradation. Biochem Biophys Res Common 359(3): 486-490.
    • (2007) Biochem Biophys Res Common , vol.359 , Issue.3 , pp. 486-490
    • Jain, R.1    Chan, M.K.2
  • 48
    • 26944443700 scopus 로고    scopus 로고
    • Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis
    • Book AJ, Yang P, Scalf M, Smith LM, Vierstra RD (2005) Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis. Plant Physiol 138(2): 1046-1057.
    • (2005) Plant Physiol , vol.138 , Issue.2 , pp. 1046-1057
    • Book, A.J.1    Yang, P.2    Scalf, M.3    Smith, L.M.4    Vierstra, R.D.5
  • 49
    • 1042289735 scopus 로고    scopus 로고
    • Clp Protease Complexes from Photosynthetic and Non-photosynthetic Plastids and Mitochondria of Plants, Their Predicted Three-dimensional Structures, and Functional Implications
    • Peltier JB, Ripoll DR, Friso G, Rudella A, Cai Y, Ytterberg J, Giacomelli L, Pillardy J, Van Wijk KJ (2004) Clp Protease Complexes from Photosynthetic and Non-photosynthetic Plastids and Mitochondria of Plants, Their Predicted Three-dimensional Structures, and Functional Implications. J Biol Chem 279(6): 4768-4781.
    • (2004) J Biol Chem , vol.279 , Issue.6 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6    Giacomelli, L.7    Pillardy, J.8    Van Wijk, K.J.9
  • 50
    • 33750969370 scopus 로고    scopus 로고
    • Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis
    • Sjogren LL, Stanne TM, Zheng B, Sutinen S, Clarke AK (2006) Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis. Plant Cell 18(10): 2635-2649.
    • (2006) Plant Cell , vol.18 , Issue.10 , pp. 2635-2649
    • Sjogren, L.L.1    Stanne, T.M.2    Zheng, B.3    Sutinen, S.4    Clarke, A.K.5
  • 51
    • 33646902709 scopus 로고    scopus 로고
    • Protein profiling of plastoglobules in chloroplasts and chromoplasts; a surprising site for differential accumulation of metabolic enzymes
    • Ytterberg AJ, Peltier JB, van Wijk KJ (2006) Protein profiling of plastoglobules in chloroplasts and chromoplasts; a surprising site for differential accumulation of metabolic enzymes. Plant Physiol 140(3): 984-997.
    • (2006) Plant Physiol , vol.140 , Issue.3 , pp. 984-997
    • Ytterberg, A.J.1    Peltier, J.B.2    van Wijk, K.J.3
  • 52
    • 10344242448 scopus 로고    scopus 로고
    • New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy
    • Peltier JB, Ytterberg AJ, Sun Q, van Wijk KJ (2004) New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. J Biol Chem 279(47): 49367-49383.
    • (2004) J Biol Chem , vol.279 , Issue.47 , pp. 49367-49383
    • Peltier, J.B.1    Ytterberg, A.J.2    Sun, Q.3    van Wijk, K.J.4
  • 54
    • 0025951229 scopus 로고
    • Tandem mass spectrometry identifies sites of three post-translational modifications of spinach light-harvesting chlorophyll protein II. Proteolytic cleavage, acetylation, and phosphorylation
    • Michel H, Griffin PR, Shabanowitz J, Hunt DF, Bennett J (1991) Tandem mass spectrometry identifies sites of three post-translational modifications of spinach light-harvesting chlorophyll protein II. Proteolytic cleavage, acetylation, and phosphorylation. J Biol Chem 266(26): 17584-17591.
    • (1991) J Biol Chem , vol.266 , Issue.26 , pp. 17584-17591
    • Michel, H.1    Griffin, P.R.2    Shabanowitz, J.3    Hunt, D.F.4    Bennett, J.5
  • 55
    • 0024296223 scopus 로고
    • Tandem mass spectrometry reveals that three photosystem II proteins of spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2 termini
    • Michel H, Hunt DF, Shabanowitz J, Bennett J (1988) Tandem mass spectrometry reveals that three photosystem II proteins of spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2 termini. J Biol Chem 263(3): 1123-1130.
    • (1988) J Biol Chem , vol.263 , Issue.3 , pp. 1123-1130
    • Michel, H.1    Hunt, D.F.2    Shabanowitz, J.3    Bennett, J.4
  • 56
    • 33646234692 scopus 로고    scopus 로고
    • Posttranslational modifications, but not transcriptional regulation, of major chloroplast RNA-binding proteins are related to Arabidopsis seedling development
    • Wang BC, Wang HX, Feng JX, Meng DZ, Qu LJ, Zhu YX (2006) Posttranslational modifications, but not transcriptional regulation, of major chloroplast RNA-binding proteins are related to Arabidopsis seedling development. Proteomics 6(8): 2555-2563.
    • (2006) Proteomics , vol.6 , Issue.8 , pp. 2555-2563
    • Wang, B.C.1    Wang, H.X.2    Feng, J.X.3    Meng, D.Z.4    Qu, L.J.5    Zhu, Y.X.6
  • 58
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP a neural networkbased method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, von Hejne G (1999) ChloroP a neural networkbased method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci 8(5): 978-984.
    • (1999) Protein Sci , vol.8 , Issue.5 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    von Hejne, G.3
  • 59
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • Polevoda B, Sherman F (2003) N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J Mol Biol 325(4): 595-622.
    • (2003) J Mol Biol , vol.325 , Issue.4 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 62
    • 33845746230 scopus 로고    scopus 로고
    • Psb27, a cyanobacterial lipoprotein, is involved in the repair cycle of photosystem II
    • Nowaczyk MM, Hebeler R, Schlodder E, Meyer HE, Warscheid B, Rogner M (2006) Psb27, a cyanobacterial lipoprotein, is involved in the repair cycle of photosystem II. Plant Cell 18(11): 3121-3131.
    • (2006) Plant Cell , vol.18 , Issue.11 , pp. 3121-3131
    • Nowaczyk, M.M.1    Hebeler, R.2    Schlodder, E.3    Meyer, H.E.4    Warscheid, B.5    Rogner, M.6
  • 63
    • 8544227718 scopus 로고    scopus 로고
    • Evidence that D1 processing is required for manganese binding and extrinsic protein assembly into photosystem II
    • Roose JL, Pakrasi HB (2004) Evidence that D1 processing is required for manganese binding and extrinsic protein assembly into photosystem II. J Biol Chem 279(44): 45417-45422.
    • (2004) J Biol Chem , vol.279 , Issue.44 , pp. 45417-45422
    • Roose, J.L.1    Pakrasi, H.B.2
  • 64
    • 33746822694 scopus 로고    scopus 로고
    • A Psb27 homologue in Arabidopsis thaliana is required for efficient repair of photodamaged photosystem, II
    • Chen H, Zhang D, Guo J, Wu H, Jin M, Lu Q, Lu C, Zhang L (2006) A Psb27 homologue in Arabidopsis thaliana is required for efficient repair of photodamaged photosystem, II. Plant Mol Biol 61(4-5): 567-575.
    • (2006) Plant Mol Biol , vol.61 , Issue.4-5 , pp. 567-575
    • Chen, H.1    Zhang, D.2    Guo, J.3    Wu, H.4    Jin, M.5    Lu, Q.6    Lu, C.7    Zhang, L.8
  • 65
    • 13444278695 scopus 로고    scopus 로고
    • Mass spectrometry for high throughput quantitative proteomics in plant research: Lessons from thylakoid membranes
    • Whitelegge JP (2004) Mass spectrometry for high throughput quantitative proteomics in plant research: lessons from thylakoid membranes. Plant Physiol Biochem 42(12): 919-927.
    • (2004) Plant Physiol Biochem , vol.42 , Issue.12 , pp. 919-927
    • Whitelegge, J.P.1
  • 66
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Hejne G, Steppuhn J, Herrmann RG (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180(3): 535-45.
    • (1989) Eur J Biochem , vol.180 , Issue.3 , pp. 535-545
    • von Hejne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 67
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation.of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias JE, Haas W, Faherty BK, Gygi SP (2005) Comparative evaluation.of mass spectrometry platforms used in large-scale proteomics investigations. Nat Methods 2(9): 667-675.
    • (2005) Nat Methods , vol.2 , Issue.9 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 68
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood JL, Tonti-Filippini JS, Gout AM, Day DA, Whelan J, Millar AH (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16(1): 241-256.
    • (2004) Plant Cell , vol.16 , Issue.1 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 69
    • 14544282417 scopus 로고    scopus 로고
    • State transitions and light adaptation require chloroplast thylakoid protein kinase STN7
    • Bellafiore S, Barneche F, Peltier G, Rochaix JD (2005) State transitions and light adaptation require chloroplast thylakoid protein kinase STN7. Nature 433(7028): 892-5.
    • (2005) Nature , vol.433 , Issue.7028 , pp. 892-895
    • Bellafiore, S.1    Barneche, F.2    Peltier, G.3    Rochaix, J.D.4
  • 70
    • 27144491327 scopus 로고    scopus 로고
    • Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases
    • Bonardi V, Pesaresi P, Becker T, Schleiff E, Wagner R, Pfannschmidt T, Jahns P, Leister D (2005) Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases. Nature 437(7062): 1179-1182.
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1179-1182
    • Bonardi, V.1    Pesaresi, P.2    Becker, T.3    Schleiff, E.4    Wagner, R.5    Pfannschmidt, T.6    Jahns, P.7    Leister, D.8
  • 71
    • 33645739638 scopus 로고    scopus 로고
    • pTAC2,-6, and - 12 are components of the transcriptionally active plastid chromosome that are required for plastid gene expression
    • Pfalz J, Liere K, Kandlbinder A, Dietz KJ, Oelmuller R (2006) pTAC2,-6, and - 12 are components of the transcriptionally active plastid chromosome that are required for plastid gene expression. Plant Cell 18(1): 176-197.
    • (2006) Plant Cell , vol.18 , Issue.1 , pp. 176-197
    • Pfalz, J.1    Liere, K.2    Kandlbinder, A.3    Dietz, K.J.4    Oelmuller, R.5
  • 73
    • 14744267531 scopus 로고    scopus 로고
    • Flux an important, but neglected, component of functional genomics
    • Fernie AR, Geigenberger P, Stitt M (2005) Flux an important, but neglected, component of functional genomics. Curr Opin Plant Biol 8(2): 174-182.
    • (2005) Curr Opin Plant Biol , vol.8 , Issue.2 , pp. 174-182
    • Fernie, A.R.1    Geigenberger, P.2    Stitt, M.3
  • 74
    • 33947713897 scopus 로고    scopus 로고
    • The N-end rule pathway for regulated proteolysis: Prokaryotic and eukaryotic strategies
    • Mogk A, Schmidt R, Bukau B (2007) The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol 17(4): 165-172.
    • (2007) Trends Cell Biol , vol.17 , Issue.4 , pp. 165-172
    • Mogk, A.1    Schmidt, R.2    Bukau, B.3
  • 75
    • 33751228400 scopus 로고    scopus 로고
    • ATP-dependent proteases of bacteria: Recognition logic and operating principles
    • Baker TA, Sauer RT (2006) ATP-dependent proteases of bacteria: recognition logic and operating principles. Trends Biochem Sci 31(12): 647-653.
    • (2006) Trends Biochem Sci , vol.31 , Issue.12 , pp. 647-653
    • Baker, T.A.1    Sauer, R.T.2
  • 77
    • 16544384619 scopus 로고    scopus 로고
    • AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes
    • Reumann S, Ma C, Lemke S, Babujee L (2004) AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes. Plant Physiol 136(1): 2587-2608.
    • (2004) Plant Physiol , vol.136 , Issue.1 , pp. 2587-2608
    • Reumann, S.1    Ma, C.2    Lemke, S.3    Babujee, L.4
  • 78
    • 0033198467 scopus 로고    scopus 로고
    • Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes
    • Amin P, Sy DA, Pilgrim ML, Parry DH, Nussaume L, Hoffman NE (1999) Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes. Plant Physiol 121(1): 61-70.
    • (1999) Plant Physiol , vol.121 , Issue.1 , pp. 61-70
    • Amin, P.1    Sy, D.A.2    Pilgrim, M.L.3    Parry, D.H.4    Nussaume, L.5    Hoffman, N.E.6
  • 79
    • 33745782714 scopus 로고    scopus 로고
    • Downregulation of ClpR2 Leads to Reduced Accumulation of the ClpPRS Protease Complex and Defects in Chloroplast Biogenesis in Arabidopsis
    • Rudella A, Friso G, Alonso JM, Ecker JR, van Wijk EJ (2006) Downregulation of ClpR2 Leads to Reduced Accumulation of the ClpPRS Protease Complex and Defects in Chloroplast Biogenesis in Arabidopsis. Plant Cell 18(7): 1704-1721.
    • (2006) Plant Cell , vol.18 , Issue.7 , pp. 1704-1721
    • Rudella, A.1    Friso, G.2    Alonso, J.M.3    Ecker, J.R.4    van Wijk, E.J.5
  • 80
    • 39049185411 scopus 로고    scopus 로고
    • Isolation of chloroplast proteins from Arabidopsis thatiana for proteome analysis
    • van Wijk KJ, Peltier JB, Giacomelli L (2007) Isolation of chloroplast proteins from Arabidopsis thatiana for proteome analysis. Methods Mol Biol 355: 43-48.
    • (2007) Methods Mol Biol , vol.355 , pp. 43-48
    • van Wijk, K.J.1    Peltier, J.B.2    Giacomelli, L.3
  • 81
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68(5): 850-858.
    • (1996) Anal Chem , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4


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